Abstract: Chimeric gene formed by the DNA sequences that encode the antigenic determinants of four proteins of L. infantum, useful for the serological diagnosis of canine Leishmaniosis and protein obtained, that consists of the prior employment of a cloning strategy. The patent describes the intermediate products generated during the process. A clone is achieved expressed in the protein rLiPO-Ct-Q (pPQI). To this initial vector, by means of the use of suitable restriction targets, DNA fragments are sequentially added that are encoded in other proteins and after each cloning step the correct orientation of each one of the inserts reduces the size of the expression products, the complete nucleotide sequence of the final pPQV clone being determined. A polypeptide is obtained with a molecular mass of 38 kD and with an isoelectric point of 7.37.

Abstract: Chimeric gene formed by the DNA sequences that encode the antigenic determinants of four proteins of L. infantum, useful for the serological diagnosis of canine Leishmaniosis and protein obtained, that consists of the prior employment of a cloning strategy. A clone is obtained which expresses the protein rLiPO-Ct-Q (pPQI). To this initial vector, by means of the use of suitable restriction targets, DNA fragments are sequentially added that are encoded in other proteins and after each cloning step the correct orientation of each one of the inserts reduces the size of the expression products, the complete nucleotide sequence of the final pPQV clone being determined. A chimeric polypeptide encoded by the chimeric gene is obtained with a molecular mass of 38 kD and with an isoelectric point of 7.37. This chimeric polypeptide is useful for preventing and/or treating leishmaniosis in animals or humans.

Abstract: The present invention relates to a process for the controlled enzymatic cleavage of purified and depigmented active allergenic proteins from indoor and outdoor source materials, which process produces fragments of allergens that retain the natural T-lymphocyte stimulating epitopes, but are depleted of IgE-binding B-cell epitopes and complement-activating agents. The invention also relates to the new pharmaceutical products. These allergen fragments do not exhibit the disadvantages of conventional allergenic extracts for immunotherapy and can be safely used to induce a state of specific T-cell anergy and immunological tolerance in allergic human beings.

Abstract: Chimeric gene formed by the DNA sequences that encode the antigenic determinants of four proteins of L. infantum, useful for the serological diagnosis of canine Leishmaniosis and protein obtained, that consists of the prior employment of a cloning strategy. The patent describes the intermediate products generated during the process. A clone is achieved expressed in the protein rLiPO-Ct-Q (pPQI). To this initial vector, by means of the use of suitable restriction targets, DNA fragments are sequentially added that are encoded in other proteins and after each cloning step the correct orientation of each one of the inserts reduces the size of the expression products, the complete nucleotide sequence of the final pPQV clone being determined. A polypeptide is obtained with a molecular mass of 38 kD and with an isoelectric point of 7.37.

Abstract: A chimeric polypeptide encoded by a chimeric gene formed by DNA sequences that encode four antigenic determinants of L. infantum is disclosed. These antigenic determinants are obtained from rLiP2a, rLiP2b, rLiH2A and rLiPO. The protein obtained, has a molecular mass of 38 KD with an isoelectric point of 7.37. This chimeric polypeptide is useful for diagnosing, preventing and/or treating leishmaniosis in animals or humans.

Abstract: A chimeric polypeptide encoded by the chimeric gene formed by the DNA sequences that encode the antigenic determinants of four proteins of L. infantum is disclosed. The protein obtained, rLiPO-Ct-Q (pPQI) has a molecular mass of 38 kD with an isoelectric point of 7.37. This chimeric polypeptide is useful for preventing and/or treating leishmaniosis in animals or humans.

Abstract: The present invention relates to a process for the controlled enzymatic cleavage of purified and depigmented active allergenic proteins from indoor and outdoor source materials, which process produces fragments of allergens that retain the the natural T-lymphocyte stimulating epitopes, but are depleted of IgE-binding B-cell epitopes and complement-activating agents. The invention also relates to the new pharmaceutical products. These allergen fragments do not exhibit the disadvantages of conventional allergenic extracts for immunotherapy and can be safely used to induce a state of specific T-cell anergy and immunological tolerance in allergic human beings.

Abstract: The invention concerns the removal of various allergologically irrelevant low-molecular weight components from the usual aqueous extracts of allergenically active proteins of plant pollens. Described are the desorption and subsequent elimination, from traditionally prepared allergenic pollen protein extracts, of low-molecular weight pigment and other compounds which are normally retained by strong electrostatic and/or hydrophobic forces. The preparation of such depigmented pollen proteins does not impair their allergenic potency or immunological specificity. The invention enables the production of fully active allergenic pollen proteins devoid of adhering low-molecular weight substances interfering with their safety, diagnostic accuracy and clinical efficacy. The purified pollen proteins represent improved starting materials for chemical derivatization, i.e. the preparation of attenuated vaccines for immunotherapy.